Evidence map›Paper›PMID 18430213›Full record

ArticleBMC plant biology2008

Characterisation of the tryptophan synthase alpha subunit in maize.

Verena Kriechbaumer, Linda Weigang, Andreas Fiesselmann, Thomas Letzel, Monika Frey, Alfons Gierl, Erich Glawischnig

Open access · goldAbstract read
In one paragraph

Article in BMC plant biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed, 1 pooled it
5.6field-weighted citation impact, top 5% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

26 citing papers in PubMed, 1 synthesis or guideline pooled it, 65 citations in OpenAlex.

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  13. Quaternary Structure of the Tryptophan Synthase α-Subunit Homolog BX1 fromJournal of the American Society for Mass Spectrometry · 2020
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 1 institution in 1 country.

Verena KriechbaumerLehrstuhl für Genetik, Technische Universität München, D-85350 Freising, Germany. verena.kriechbaumer@wzw.tum.de
Linda Weigang
Andreas Fiesselmann
Thomas Letzel
Monika Frey
Alfons Gierl
Erich Glawischnig
Technical University of Munich · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundIn bacteria, such as Salmonella typhimurium, tryptophan is synthesized from indole-3-glycerole phosphate (IGP) by a tryptophan synthase alphabetabetaalpha heterotetramer. Plants have evolved multiple alpha (TSA) and beta (TSB) homologs, which have probably diverged in biological function and their ability of subunit interaction. There is some evidence for a tryptophan synthase (TS) complex in Arabidopsis. On the other hand maize (Zea mays) expresses the TSA-homologs BX1 and IGL that efficiently cleave IGP, independent of interaction with TSB.

resultsIn order to clarify, how tryptophan is synthesized in maize, two TSA homologs, hitherto uncharacterized ZmTSA and ZmTSAlike, were functionally analyzed. ZmTSA is localized in plastids, the major site of tryptophan biosynthesis in plants. It catalyzes the tryptophan synthase alpha-reaction (cleavage of IGP), and forms a tryptophan synthase complex with ZmTSB1 in vitro. The catalytic efficiency of the alpha-reaction is strongly enhanced upon complex formation. A 160 kD tryptophan synthase complex was partially purified from maize leaves and ZmTSA was identified as native alpha-subunit of this complex by mass spectrometry. ZmTSAlike, for which no in vitro activity was detected, is localized in the cytosol. ZmTSAlike, BX1, and IGL were not detectable in the native tryptophan synthase complex in leaves.

conclusionIt was demonstrated in vivo and in vitro that maize forms a tryptophan synthase complex and ZmTSA functions as alpha-subunit in this complex.

Indexed as

Amino Acid SequenceCell ExtractsChromatography, GelGreen Fluorescent ProteinsKineticsMolecular Sequence DataPeptidesPlant LeavesPlant ProteinsProtein SubunitsProtein TransportRecombinant ProteinsSequence Homology, Amino AcidSubcellular FractionsTryptophan SynthaseZea maysCell Extractsenhanced green fluorescent proteinGreen Fluorescent ProteinsPeptidesPlant ProteinsProtein SubunitsRecombinant ProteinsTryptophan Synthase

Identifiers

PMID18430213
PMCPMC2395261
OpenAlexW2134381712

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LicenceCC BY
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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.